We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1w1w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
A multisubunit complex called cohesin forms a huge ring structure that, mediates sister chromatid cohesion, possibly by entrapping sister DNAs, following replication. Cohesin's kleisin subunit Scc1 completes the ring, connecting the ABC-like ATPase heads of a V-shaped Smc1/3 heterodimer., Proteolytic cleavage of Scc1 by separase triggers sister chromatid, disjunction, presumably by breaking the Scc1 bridge. One half of the, SMC-kleisin bridge is revealed here by a crystal structure of Smc1's, ATPase complexed with Scc1's C-terminal domain. The latter forms a winged, helix that binds a pair of beta strands in Smc1's ATPase head. Mutation of, conserved residues within the contact interface destroys Scc1's, interaction with Smc1/3 heterodimers and eliminates cohesin function., Interaction of Scc1's N terminus with Smc3 depends on prior C terminus, connection with Smc1. There is little or no turnover of Smc1-Scc1, interactions within cohesin complexes in vivo because expression of, noncleavable Scc1 after DNA replication does not hinder anaphase.
+
A multisubunit complex called cohesin forms a huge ring structure that mediates sister chromatid cohesion, possibly by entrapping sister DNAs following replication. Cohesin's kleisin subunit Scc1 completes the ring, connecting the ABC-like ATPase heads of a V-shaped Smc1/3 heterodimer. Proteolytic cleavage of Scc1 by separase triggers sister chromatid disjunction, presumably by breaking the Scc1 bridge. One half of the SMC-kleisin bridge is revealed here by a crystal structure of Smc1's ATPase complexed with Scc1's C-terminal domain. The latter forms a winged helix that binds a pair of beta strands in Smc1's ATPase head. Mutation of conserved residues within the contact interface destroys Scc1's interaction with Smc1/3 heterodimers and eliminates cohesin function. Interaction of Scc1's N terminus with Smc3 depends on prior C terminus connection with Smc1. There is little or no turnover of Smc1-Scc1 interactions within cohesin complexes in vivo because expression of noncleavable Scc1 after DNA replication does not hinder anaphase.
==About this Structure==
==About this Structure==
Line 26: Line 26:
[[Category: mitosis]]
[[Category: mitosis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:18:15 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:33 2008''

Revision as of 13:39, 21 February 2008

Image:1w1w.gif

1w1w, resolution 2.9Å

Drag the structure with the mouse to rotate

SC SMC1HD:SCC1-C COMPLEX, ATPGS

Overview

A multisubunit complex called cohesin forms a huge ring structure that mediates sister chromatid cohesion, possibly by entrapping sister DNAs following replication. Cohesin's kleisin subunit Scc1 completes the ring, connecting the ABC-like ATPase heads of a V-shaped Smc1/3 heterodimer. Proteolytic cleavage of Scc1 by separase triggers sister chromatid disjunction, presumably by breaking the Scc1 bridge. One half of the SMC-kleisin bridge is revealed here by a crystal structure of Smc1's ATPase complexed with Scc1's C-terminal domain. The latter forms a winged helix that binds a pair of beta strands in Smc1's ATPase head. Mutation of conserved residues within the contact interface destroys Scc1's interaction with Smc1/3 heterodimers and eliminates cohesin function. Interaction of Scc1's N terminus with Smc3 depends on prior C terminus connection with Smc1. There is little or no turnover of Smc1-Scc1 interactions within cohesin complexes in vivo because expression of noncleavable Scc1 after DNA replication does not hinder anaphase.

About this Structure

1W1W is a Protein complex structure of sequences from Saccharomyces cerevisiae with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structure and stability of cohesin's Smc1-kleisin interaction., Haering CH, Schoffnegger D, Nishino T, Helmhart W, Nasmyth K, Lowe J, Mol Cell. 2004 Sep 24;15(6):951-64. PMID:15383284

Page seeded by OCA on Thu Feb 21 15:39:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w1w"
Personal tools